Header list of 1do9.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 20-DEC-99 1DO9 TITLE SOLUTION STRUCTURE OF OXIDIZED MICROSOMAL RABBIT CYTOCHROME B5. TITLE 2 FACTORS DETERMINING THE HETEROGENEOUS BINDING OF THE HEME. COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME B5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SOLUBLE DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_COMMON: RABBIT; SOURCE 4 ORGANISM_TAXID: 9986; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKK223 KEYWDS CYTOCHROME, HEME, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 40 AUTHOR L.BANCI,I.BERTINI,A.ROSATO,S.SCACCHIERI REVDAT 4 16-FEB-22 1DO9 1 REMARK LINK REVDAT 3 24-FEB-09 1DO9 1 VERSN REVDAT 2 20-MAR-00 1DO9 1 JRNL REMARK REVDAT 1 05-JAN-00 1DO9 0 JRNL AUTH L.BANCI,I.BERTINI,A.ROSATO,S.SCACCHIERI JRNL TITL SOLUTION STRUCTURE OF OXIDIZED MICROSOMAL RABBIT CYTOCHROME JRNL TITL 2 B5. FACTORS DETERMINING THE HETEROGENEOUS BINDING OF THE JRNL TITL 3 HEME. JRNL REF EUR.J.BIOCHEM. V. 267 755 2000 JRNL REFN ISSN 0014-2956 JRNL PMID 10651812 JRNL DOI 10.1046/J.1432-1327.2000.01054.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 MODIFIED FOR USING PSEUDOCONTACT SHIFTS REMARK 3 AS CONSTRAINTS, AMBER 4.0 REMARK 3 AUTHORS : GUENTERT (DYANA), KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DO9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-99. REMARK 100 THE DEPOSITION ID IS D_1000010245. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : PH 7, 2-3 MM PROTEIN, 1MM REMARK 210 PHOSPHATE BUFFER; PH 7, 2-3 MM REMARK 210 PROTEIN, 1MM PHOSPHATE BUFFER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D TOCSY; 3D_ REMARK 210 15N-SEPARATED_TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 150 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 25 ALA A 67 CA ALA A 67 CB 0.259 REMARK 500 39 ALA A 67 CA ALA A 67 CB 0.334 REMARK 500 39 ALA A 67 CA ALA A 67 C 0.171 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 2 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 4 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 12 PHE A 74 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES REMARK 500 16 ASP A 1 CB - CA - C ANGL. DEV. = 17.2 DEGREES REMARK 500 16 ASP A 1 N - CA - CB ANGL. DEV. = -15.5 DEGREES REMARK 500 16 ASP A 1 N - CA - C ANGL. DEV. = -20.4 DEGREES REMARK 500 17 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 24 ALA A 67 CB - CA - C ANGL. DEV. = 15.6 DEGREES REMARK 500 25 ALA A 67 CB - CA - C ANGL. DEV. = 20.1 DEGREES REMARK 500 25 ALA A 67 O - C - N ANGL. DEV. = -10.6 DEGREES REMARK 500 26 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 27 ASP A 1 N - CA - CB ANGL. DEV. = -10.9 DEGREES REMARK 500 28 PHE A 74 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES REMARK 500 34 ASP A 1 CB - CA - C ANGL. DEV. = 18.2 DEGREES REMARK 500 34 ASP A 1 N - CA - CB ANGL. DEV. = -13.0 DEGREES REMARK 500 34 ASP A 1 N - CA - C ANGL. DEV. = -21.1 DEGREES REMARK 500 35 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 37 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 39 ALA A 67 CB - CA - C ANGL. DEV. = 20.1 DEGREES REMARK 500 39 ALA A 67 O - C - N ANGL. DEV. = -10.6 DEGREES REMARK 500 39 LEU A 94 CB - CA - C ANGL. DEV. = 14.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 TYR A 6 110.36 -31.88 REMARK 500 1 HIS A 17 -65.83 -125.56 REMARK 500 1 SER A 18 -42.53 172.55 REMARK 500 1 SER A 20 26.08 -151.20 REMARK 500 1 THR A 21 92.82 -47.52 REMARK 500 1 HIS A 26 78.93 61.66 REMARK 500 1 HIS A 27 46.50 32.64 REMARK 500 1 GLU A 43 -45.75 -154.38 REMARK 500 1 LYS A 86 -70.06 -155.22 REMARK 500 1 SER A 88 84.03 -154.27 REMARK 500 1 PRO A 90 -169.55 -76.15 REMARK 500 1 GLU A 92 139.68 64.71 REMARK 500 2 TYR A 6 92.55 -52.29 REMARK 500 2 ASN A 16 29.78 -156.57 REMARK 500 2 LYS A 19 -22.32 171.75 REMARK 500 2 SER A 20 59.73 -149.69 REMARK 500 2 THR A 21 81.71 -66.03 REMARK 500 2 HIS A 26 79.07 70.48 REMARK 500 2 HIS A 27 45.93 30.03 REMARK 500 2 HIS A 63 156.39 -49.45 REMARK 500 2 HIS A 80 107.50 -58.90 REMARK 500 2 LYS A 86 43.37 -140.33 REMARK 500 2 SER A 88 63.56 -164.71 REMARK 500 2 MET A 91 177.72 53.58 REMARK 500 3 LYS A 2 -57.64 -146.65 REMARK 500 3 VAL A 4 -126.97 -108.78 REMARK 500 3 TYR A 6 97.95 44.58 REMARK 500 3 HIS A 15 -118.71 -80.42 REMARK 500 3 ASN A 16 50.99 39.44 REMARK 500 3 SER A 18 -83.11 56.03 REMARK 500 3 LYS A 19 -70.88 -87.11 REMARK 500 3 SER A 20 92.57 -45.33 REMARK 500 3 HIS A 26 77.34 71.53 REMARK 500 3 HIS A 27 44.17 31.19 REMARK 500 3 HIS A 63 154.46 -49.81 REMARK 500 3 HIS A 80 151.13 -49.25 REMARK 500 3 ASP A 82 -31.92 167.26 REMARK 500 3 LYS A 86 -41.21 -161.54 REMARK 500 3 LEU A 87 99.60 -62.35 REMARK 500 3 SER A 88 174.77 58.47 REMARK 500 3 LYS A 89 86.36 -157.52 REMARK 500 4 VAL A 4 -134.91 -113.23 REMARK 500 4 TYR A 6 90.85 38.95 REMARK 500 4 HIS A 15 -107.71 -95.60 REMARK 500 4 LYS A 19 -30.91 -176.46 REMARK 500 4 HIS A 26 73.60 89.45 REMARK 500 4 HIS A 27 50.78 30.32 REMARK 500 4 LEU A 36 -74.37 -50.01 REMARK 500 4 GLU A 43 -39.58 -138.88 REMARK 500 4 HIS A 63 165.60 53.48 REMARK 500 REMARK 500 THIS ENTRY HAS 554 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 5 TYR A 7 0.07 SIDE CHAIN REMARK 500 29 TYR A 30 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM A 95 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 39 NE2 REMARK 620 2 HEM A 95 NA 91.0 REMARK 620 3 HEM A 95 NB 93.6 89.1 REMARK 620 4 HEM A 95 NC 89.2 178.7 89.6 REMARK 620 5 HEM A 95 ND 87.5 91.5 178.8 89.8 REMARK 620 6 HIS A 63 NE2 174.7 92.2 90.6 87.7 88.3 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 95 DBREF 1DO9 A 1 94 UNP P00169 CYB5_RABIT 6 99 SEQRES 1 A 94 ASP LYS ASP VAL LYS TYR TYR THR LEU GLU GLU ILE LYS SEQRES 2 A 94 LYS HIS ASN HIS SER LYS SER THR TRP LEU ILE LEU HIS SEQRES 3 A 94 HIS LYS VAL TYR ASP LEU THR LYS PHE LEU GLU GLU HIS SEQRES 4 A 94 PRO GLY GLY GLU GLU VAL LEU ARG GLU GLN ALA GLY GLY SEQRES 5 A 94 ASP ALA THR GLU ASN PHE GLU ASP VAL GLY HIS SER THR SEQRES 6 A 94 ASP ALA ARG GLU LEU SER LYS THR PHE ILE ILE GLY GLU SEQRES 7 A 94 LEU HIS PRO ASP ASP ARG SER LYS LEU SER LYS PRO MET SEQRES 8 A 94 GLU THR LEU HET HEM A 95 73 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 2 HEM C34 H32 FE N4 O4 HELIX 1 1 THR A 8 LYS A 13 1 6 HELIX 2 2 THR A 33 LEU A 36 5 4 HELIX 3 3 GLU A 43 GLN A 49 1 7 HELIX 4 4 ALA A 54 GLY A 62 1 9 HELIX 5 5 SER A 64 PHE A 74 1 11 HELIX 6 6 HIS A 80 ARG A 84 5 5 SHEET 1 A 3 TRP A 22 ILE A 24 0 SHEET 2 A 3 LYS A 28 ASP A 31 -1 N TYR A 30 O LEU A 23 SHEET 3 A 3 ILE A 75 GLU A 78 -1 N ILE A 76 O VAL A 29 LINK NE2 HIS A 39 FE HEM A 95 1555 1555 2.01 LINK NE2 HIS A 63 FE HEM A 95 1555 1555 2.01 SITE 1 AC1 13 PHE A 35 HIS A 39 PRO A 40 VAL A 45 SITE 2 AC1 13 LEU A 46 ALA A 54 ASN A 57 VAL A 61 SITE 3 AC1 13 HIS A 63 ALA A 67 LEU A 70 SER A 71 SITE 4 AC1 13 PHE A 74 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - b 16 2 Bytes